| Literature DB >> 17401647 |
Timo T Myöhänen1, Jarkko I Venäläinen, Erkki Tupala, J Arturo Garcia-Horsman, Riitta Miettinen, Pekka T Männistö.
Abstract
Prolyl oligopeptidase (POP) is a serine endoprotease that hydrolyses peptides shorter than 30-mer. POP may have a role in inositol 1,4,5-triphosphate (IP(3)) signaling and in the actions of antidepressants, and POP inhibitors have exhibited antiamnesic and neuroprotective properties. However, little is known about the distribution of POP protein in the brain. We used immunohistochemistry to localize POP enzyme in the human whole hemisphere and in the rat whole brain. In humans, the highest POP densities were observed in caudate nucleus and putamen, hippocampus and cortex. In the rat, the highest POP densities were found in substantia nigra, hippocampus, cerebellum and caudate putamen. In general, the distribution of POP in human and rat brains was very similar and resembled that of IP(3) receptors. Our findings are support for a role of POP in movement regulation, cognition and possibly in IP(3) signaling. The expression of POP in processing nuclei further supports its function beyond neuropeptide metabolism.Entities:
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Year: 2007 PMID： 17401647 DOI： 10.1007/s11064-007-9316-y
Source DB: PubMed Journal: Neurochem Res ISSN： 0364-3190 Impact factor: 3.996